Antibacterial Action of Melittin, a Polypeptide from Bee Venom

Fennell, Jean F.; Shipman, William H.; Cole, Leonard J.

doi:10.3181/00379727-127-32779

Cited by 82 publications

(60 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The antibacterial properties of bee venom as a natural antibacterial agent have been extensively studied, and bee venom therapy has been suggested to be used as an alternative to antibiotic therapy (Fennell et al, 1968;Somerfield et al, 1984;Saini et al, 1997). A strong antibacterial activity of bee venom against both Gramnegative and Gram positive bacteria had been reported (Stocker and Traynor, 1986;Perumal Samy et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

The Antifungal Activity of Bee Venom against Dermatophytes

Yu¹,

Kim²,

Park³

et al. 2012

Journal of Applied Biological Chemistry

View full text Add to dashboard Cite

The antifungal activities of the bee venom against Trichophyton mentagrophytes and Trichophyton rubrum were determined by using modified broth dilution assay. The most common dermatophytes, named T. mentagrophytes and T. rubrum, were known to cause a variety of cutaneous infections in humans and animals. The bee venom exhibited prominent antifungal activities against the two dermatophytes tested in this investigation. Moreover, the antifungal activities of the bee venom were much stronger than that of fluconazole, one of the commercial antifungal drugs used in the treatment and prevention of superficial and systemic fungal infections. The result suggests that bee venom could be developed as a natural antifungal drug.

show abstract

Section: Discussionmentioning

confidence: 99%

The Antifungal Activity of Bee Venom against Dermatophytes

Yu¹,

Kim²,

Park³

et al. 2012

Journal of Applied Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…8]. Ten of the 15 peptoids exhibited low-micromolar MICs against both E. coli and B. subtilis, demonstrating that nonnatural peptoid oligomers can be as active as some antimicrobial peptides (MICs for pexiganan (44)-a selective AMP analog of magainin-2-and the bee-venom AMP melittin (45) are shown in Table 1). …”

Section: Resultsmentioning

confidence: 99%

Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides

Chongsiriwatana¹,

Patch²,

Czyzewski³

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

573

578

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) and their mimics are emerging as promising antibiotic agents. We present a library of ''ampetoids'' (antimicrobial peptoid oligomers) with helical structures and biomimetic sequences, several members of which have low-micromolar antimicrobial activities, similar to cationic AMPs like pexiganan. Broad-spectrum activity against six clinically relevant BSL2 pathogens is also shown. This comprehensive structure-activity relationship study, including circular dichroism spectroscopy, minimum inhibitory concentration assays, hemolysis and mammalian cell toxicity studies, and specular x-ray reflectivity measurements shows that the in vitro activities of ampetoids are strikingly similar to those of AMPs themselves, suggesting a strong mechanistic analogy. The ampetoids' antibacterial activity, coupled with their low cytotoxicity against mammalian cells, make them a promising class of antimicrobials for biomedical applications. Peptoids are biostable, with a protease-resistant N-substituted glycine backbone, and their sequences are highly tunable, because an extensive diversity of side chains can be incorporated via facile solid-phase synthesis. Our findings add to the growing evidence that nonnatural foldamers will emerge as an important class of therapeutics.antibiotics ͉ peptidomimetics ͉ structure-activity studies N atural antimicrobial peptides (AMPs) defend a wide array of organisms against bacterial pathogens and show potential as supplements for or replacements of conventional antibiotics, because few bacteria have evolved resistance to them (1-3). Many AMPs kill bacteria by permeabilization of the cytoplasmic membrane, causing depolarization, leakage, and death (4), whereas others target additional anionic bacterial constituents (e.g., DNA, RNA, or cell wall components) (2, 5). Amphipathic secondary structures in which residues are segregated into hydrophobic and cationic regions ( Fig. 1 A and B) are the hallmark of most AMPs (6). Regardless of their final target of killing, AMPs must interact with the bacterial cytoplasmic membrane, and their amphipathicity is integral to such interactions (1, 2, 7). Additionally, their cationic nature imparts AMPs with some measure of selectivity, because mammalian cell membranes are largely zwitterionic. The precise nature of AMP-membrane interactions remains controversial and actively debated; a variety of mechanisms have been proposed, including the carpet (4), barrel-stave pore (4), toroidal pore (8), and aggregate (9) models. Nevertheless, a considerable number of structure-activity investigations have elucidated how the physicochemical properties of these molecules relate to their biological activities (4,7,(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22).Although AMPs have been actively studied for decades (23-25), they have yet to see widespread clinical use (1). This is due in part to the vulnerability of many peptide therapeutics to rapid in vivo degradation, which dramatically reduces their bioavailability. Nonnatural mimics of AMPs...

show abstract

“…It can interact strongly with lipid bilayer membranes and disrupt them (Papo and Shai, 2003;Higashino et al, 2001;Sessa et al, 1969). Other biological functions such as hemolysis (Hincha et al, 1996), antitumors (Winder et al, 1998), protection against irradiation (Ginsberg et al, 1968) and antibacterial properties (Fennell et al, 1968) are also well documented. Furthermore, melittin inhibits the activities of Na + -ATPase, K + -ATPase and Ca + -ATPase (Cuppoletti and Abbott, 1990;Raynor et al, 1991) using different mechanisms (Murtazina et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Expression of melittin gene in the venom gland of the Chinese honeybee, Apis cerana cerana

Zhang

Tang

2005

Apidologie

View full text Add to dashboard Cite

-Melittin is the principal component of bee venom. Melittin in Apis cerana (Ac-melt) is a single copy gene. A full length Ac-melt cDNA is 389 bp, with a single 191 bp intron in the genome. Its mRNA level was high during the first week of adult life and low during the rest of adult life. Melittin or its precursor could not be detected in the pupal stage. Melittin level increased rapidly to its maximum (about 95 µg per worker bee) during the first 8-10 days of adult age, and remained constant for about 20 days before starting to decline slowly. The expression of melittin is regulated at the transcriptional level. Melittin / gene expression / venom gland / Apis cerana

show abstract

Antibacterial Action of Melittin, a Polypeptide from Bee Venom

Cited by 82 publications

References 0 publications

The Antifungal Activity of Bee Venom against Dermatophytes

The Antifungal Activity of Bee Venom against Dermatophytes

Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides

Expression of melittin gene in the venom gland of the Chinese honeybee, Apis cerana cerana

Contact Info

Product

Resources

About